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KMID : 0620920100420040310
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Experimental & Molecular Medicine
2010 Volume.42 No. 4 p.310 ~ p.318
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Differential alternative splicing of human transglutaminase 4 in benign prostate hyperplasia and prostate cancer
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Cho Sung-Yup
Choi Kyung-Ho
Jeon Ju-Hong
Kim Chai-Wan
Shin Dong-Myung
Lee Jong-Bouk
Lee Sang-Eun
Kim Choung-Soo
Park Jeong-Soo
Jeong Eui-Man
Jang Gi-Yong
Song Kye-Yong
Kim In-Gyu
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Abstract
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Transglutaminase 4 is a member of enzyme family that catalyzes calcium-dependent posttranslational modification of proteins. Although transglutaminase 4 has been shown to have prostate-restricted expression pattern, little is known about the biological function of transglutaminase 4 in human. To gain insight into its role in prostate, we analyzed the expression status of human transglutaminase 4 in benign prostate hyperplasia (BPH) and prostate cancer (PCa). Unexpectedly, RT-PCR and nucleotide sequence analysis showed four alternative splicing variants of transglutaminase 4: transglutaminase 4-L, -M (-M1 and -M2) and -S. The difference between transglutaminase 4-M1 and -M2 is attributed to splicing sites, but not nucleotide size. The deduced amino acid sequences showed that transglutaminase 4-L, -M1 and -M2 have correct open reading frames, whereas transglutaminase 4-S has a truncated reading frame. RT-PCR analysis of clinical samples revealed that transglutaminase 4-M and -S were detected in all tested prostate tissue (80 BPH and 48 PCa). Interestingly, transglutaminase 4-L was found in 56% of BPH (45 out of 80) and only in 15% of PCa (7 out of 48). However, transglutaminase 4-L expression did not correlate with serum prostate-specific antigen (PSA) level, prostate volumes or PSA densities. These results will provide a clue to future investigation aiming at delineating physiological and pathological roles of human transglutaminase 4.
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KEYWORD
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alternative splicing, prostate hyperplasia, prostatic neoplasms, transglutaminase 4
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